ID A0A1V6P9X3_PENDC Unreviewed; 1215 AA.
AC A0A1V6P9X3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENDEC_c013G02490 {ECO:0000313|EMBL:OQD73791.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD73791.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD73791.1}.
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DR EMBL; MDYL01000013; OQD73791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6P9X3; -.
DR STRING; 69771.A0A1V6P9X3; -.
DR OMA; CTMHTST; -.
DR OrthoDB; 2253151at2759; -.
DR Proteomes; UP000191522; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000191522}.
FT DOMAIN 361..519
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 710..943
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1067..1189
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1031..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1118
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1215 AA; 135046 MW; 149F79CBB701ABE4 CRC64;
MNGPGDDNSD KKKILAQALS EPKSLCILSD AKIEISTVTE LPPSKLKFPQ LSDTTERIFP
IRSVLSFDSN PSSALQTPSL DKLETPFSPI TDAIQNNGII GIGSIKRPNY LARMHKERGS
YSGVSPSLPI VPTLGNPFPE SGINSPNSRS PVQSLSLQEQ LQQTLREGGR ILDISRKTRG
LQYSHEDEAT PMIQSFGALL VISESGDDLT VQIASSNSKS ILGYTPDELF ELKSICSILP
GSQQSIFLSH VRLVLDDEYD VEISGPEVFD LSIATMAGET KRLWCTMHTS NAYKNYVICE
LEHEHGIESS QDILPRDTLQ SDGEIGDRQP SKALDQRTAT LNSELLNDLP RILQRIACAQ
TLKDLVRNAI LNLQQWISFH RVSMFHFDGD RNGLVIADIA DQSLGLDSYE GIHFEESAFP
DDLKRQYLRN PVSFSYRRRD EVAELVYRLS TNRSGLDLSH CYLPVAESTK NTNDMSMQAC
ISIGIYVFGK LWGLILCQSY DADLRPHPLL QKVCWFMSEA VSSNIERLSY TLPFQLEEQS
VSSGDTDSNN VKSPSGDLLC LFGADYAAAS ILGETKILGR PFDSQEVLAL LEYLRAKELD
TVLWSTDIIP DFEDLDYSPG FRHLSGFLYI PLSANGQDFI IFFRSNKQEN SQSLSAQHGL
EKTTRQAEWS AAQFAKASIL SLLYRTFSEI WQEKEAAMQN NQLMRLLLAN SAHEFRTPLN
AIINYLEIAL DGNLVPETRE NLSRSHSASK SLVYIINDLL DLTNAENGQS LIKDEVFSLS
ETLCEATDIF WEEARQKHVD LQVVQHAALP PVLGDQRRVR QAITNLISNA VQHTTSGAVT
IESCVPSDCW KPGHITVEVA IHDTGSGMSS QTVEALFCEL EQVSNSGYMR NPKYGKNEVE
TESVLGLGLA LVARIVRNMN GQLSLKSEEG KGSCFKIRLN FPLPEKSDAS ASASVSASAS
QAKEDSTGHE ACNIQHNSAQ GEQTDKDKVR KSNEVKEGIP CHCGDETFPS TNFLDIDASL
DSGESRTLTL PLHQQKEHST TPVPNPSTDT PDPKSTPTDM PRPSQLRILV AEDDPINSCI
VQKRLEKLGY QVRLTANGKE CSSLYIEWPH SFDAILMDLQ MPIVNGTSAT KIIRDHEAQF
FENCSIPIFA VSASLKESDR QSYIDAGFNG WIMKPIDFQR VDKLLRGVED RELKETCLYK
HCTWEQGGWL ESSDE
//
